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Items: 1 to 20 of 33

1.

A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution.

Strobl S, Maskos K, Wiegand G, Huber R, Gomis-Rüth FX, Glockshuber R.

Structure. 1998 Jul 15;6(7):911-21.

PMID:
9687373
2.

Properties and applications of starch-converting enzymes of the alpha-amylase family.

van der Maarel MJ, van der Veen B, Uitdehaag JC, Leemhuis H, Dijkhuizen L.

J Biotechnol. 2002 Mar 28;94(2):137-55. Review.

PMID:
11796168
3.

Structural basis for the inhibition of mammalian and insect alpha-amylases by plant protein inhibitors.

Payan F.

Biochim Biophys Acta. 2004 Feb 12;1696(2):171-80. Review.

PMID:
14871658
4.
5.
6.

Amylolytic enzymes: molecular aspects of their properties.

Horváthová V, Janecek S, Sturdík E.

Gen Physiol Biophys. 2001 Mar;20(1):7-32. Review.

PMID:
11508823
7.

Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.

Franco OL, Rigden DJ, Melo FR, Grossi-De-Sá MF.

Eur J Biochem. 2002 Jan;269(2):397-412. Review.

8.

Porcine pancreatic alpha-amylase inhibition by the kidney bean (Phaseolus vulgaris) inhibitor (alpha-AI1) and structural changes in the alpha-amylase inhibitor complex.

Santimone M, Koukiekolo R, Moreau Y, Le Berre V, Rougé P, Marchis-Mouren G, Desseaux V.

Biochim Biophys Acta. 2004 Feb 12;1696(2):181-90. Review.

PMID:
14871659
9.

Proteinaceous alpha-amylase inhibitors.

Svensson B, Fukuda K, Nielsen PK, Bønsager BC.

Biochim Biophys Acta. 2004 Feb 12;1696(2):145-56. Review.

PMID:
14871655
10.

Structural features, substrate specificity, kinetic properties of insect α-amylase and specificity of plant α-amylase inhibitors.

Kaur R, Kaur N, Gupta AK.

Pestic Biochem Physiol. 2014 Nov;116:83-93. doi: 10.1016/j.pestbp.2014.09.005. Review.

PMID:
25454524
11.

alpha-Amylase family: molecular biology and evolution.

Janecek S.

Prog Biophys Mol Biol. 1997;67(1):67-97. Review. No abstract available.

PMID:
9401418
12.

[Activation, activity and inhibition of bovine trypsin].

Bode W.

Naturwissenschaften. 1979 May;66(5):251-8. Review. German.

PMID:
381946
13.

alpha-Amylase: an ideal representative of thermostable enzymes.

Prakash O, Jaiswal N.

Appl Biochem Biotechnol. 2010 Apr;160(8):2401-14. doi: 10.1007/s12010-009-8735-4. Review. Erratum in: Appl Biochem Biotechnol. 2010 Nov;162(7):2123-4.

PMID:
19763902
14.

Barley alpha-amylase/subtilisin inhibitor: structure, biophysics and protein engineering.

Nielsen PK, Bønsager BC, Fukuda K, Svensson B.

Biochim Biophys Acta. 2004 Feb 12;1696(2):157-64. Review.

PMID:
14871656
16.

α-Amylase inhibitors: a review of raw material and isolated compounds from plant source.

Sales PM, Souza PM, Simeoni LA, Silveira D.

J Pharm Pharm Sci. 2012;15(1):141-83. Review.

17.

Present-day studies on cereals protein nature alpha-amylase inhibitors.

Warchalewski JR.

Nahrung. 1983;27(2):103-17. Review. No abstract available.

PMID:
6190085
18.

Enzyme inhibitors of microbial origin.

Schindler P.

Philos Trans R Soc Lond B Biol Sci. 1980 Aug 11;290(1040):291-301. Review.

PMID:
6158062
19.

[Plant and microbial inhibitors of amylolytic enzymes (author's transl)].

Andrzejczuk-Hybel J.

Postepy Biochem. 1981;27(2):181-96. Review. Polish. No abstract available.

PMID:
6174962
20.

Biochemical features and kinetic properties of α-amylases from marine organisms.

Homaei A, Ghanbarzadeh M, Monsef F.

Int J Biol Macromol. 2016 Feb;83:306-14. doi: 10.1016/j.ijbiomac.2015.11.080. Review.

PMID:
26657843
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